ID G3GBT6_BACIU Unreviewed; 341 AA.
AC G3GBT6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN Name=fbk2 {ECO:0000313|EMBL:AEP02954.1};
OS Bacillus subtilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423 {ECO:0000313|EMBL:AEP02954.1};
RN [1] {ECO:0000313|EMBL:AEP02954.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A1 {ECO:0000313|EMBL:AEP02954.1};
RA Yong J.K.;
RT "Molecular cloning and characterization of the gene encoding a fibrinolytic
RT enzyme.";
RL World J. Microbiol. Biotechnol. 20:711-717(2004).
RN [2] {ECO:0000313|EMBL:AEP02954.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A1 {ECO:0000313|EMBL:AEP02954.1};
RA Yong J.K.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR EMBL; JF826532; AEP02954.1; -; Genomic_DNA.
DR AlphaFoldDB; G3GBT6; -.
DR MEROPS; M04.025; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR032475; Protealysin_N_PP.
DR PANTHER; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF16485; PLN_propep; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 7..44
FT /note="Protealysin N-terminal propeptide"
FT /evidence="ECO:0000259|Pfam:PF16485"
FT DOMAIN 62..170
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 173..340
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 163
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 341 AA; 37708 MW; 07067E53D82F6E9E CRC64;
MPAQRMRSVI PPYMLRRIIE HGNAPQRDCA LHTLNHVQSL LGNKPLRSPT EKNARAGEAL
RDIYDAQNGT QLPGKPVRKE GQPSNHDVAV DEAYDYLGVT YDFFWQAYHR NSLDNQGLPL
VGSVHYGKEY QNAFWNGQQM VFGDGDGEIF NRFTIAIDVV GHELAHGVTE SEAGLIYYQQ
SGALNESLSD VFGSLVKQFH LQQTADKADW LIGAGLLAKG IKGKGLRSMS APGTAYDDPL
LGKDPQPASM KDYIQTKEDN GRVHLNSGIP NRAFYLAATA LGGFAWEKAG YVWYDTVCDK
ALPQNADFAT FARATVKHAQ ARFDQSVADK VQQAWHQVGV E
//
